Characterization of nicotinamidases: steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism
…, Y Cen, TL Vrablik, P Xu, E Allen, W Hanna-Rose…
Index: French, Jarrod B.; Cen, Yana; Vrablik, Tracy L.; Xu, Ping; Allen, Eleanor; Hanna-Rose, Wendy; Sauve, Anthony A. Biochemistry, 2010 , vol. 49, # 49 p. 10421 - 10439
Full Text: HTML
Citation Number: 22
Abstract
Nicotinamidases are metabolic enzymes that hydrolyze nicotinamide to nicotinic acid. These enzymes are widely distributed across biology, with examples found encoded in the genomes of Mycobacteria, Archaea, Eubacteria, Protozoa, yeast, and invertebrates, but there are none found in mammals. Although recent structural work has improved our understanding of these enzymes, their catalytic mechanism is still not well understood. ...
Related Articles:
[Journal of Medicinal Chemistry, , vol. 43, # 16 p. 3168 - 3185]
[Journal of Medicinal Chemistry, , vol. 43, # 16 p. 3168 - 3185]
[Journal of Medicinal Chemistry, , vol. 43, # 16 p. 3168 - 3185]
[Journal of Medicinal Chemistry, , vol. 43, # 16 p. 3168 - 3185]
[Biochemistry, , vol. 49, # 49 p. 10421 - 10439]